Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes.
about
Methylated nucleosides in tRNA and tRNA methyltransferasesSubstrate tRNA Recognition Mechanism of a Multisite-specific tRNA Methyltransferase, Aquifex aeolicus Trm1, Based on the X-ray Crystal StructureThe tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmLCharacterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substratesThe structure of Rv2372c identifies an RsmE-like methyltransferase from Mycobacterium tuberculosisSubstrate recognition and modification by the nosiheptide resistance methyltransferaseThe catalytic domain of topological knot tRNA methyltransferase (TrmH) discriminates between substrate tRNA and nonsubstrate tRNA via an induced-fit process.Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases.N7-Methylguanine at position 46 (m7G46) in tRNA from Thermus thermophilus is required for cell viability at high temperatures through a tRNA modification networkYibK is the 2'-O-methyltransferase TrmL that modifies the wobble nucleotide in Escherichia coli tRNA(Leu) isoacceptors.tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily.Diversity in mechanism and function of tRNA methyltransferases.Subcellular localization and RNA interference of an RNA methyltransferase gene from silkworm, Bombyx mori.Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes.Transfer RNA methyltransferases with a SpoU-TrmD (SPOUT) fold and their modified nucleosides in tRNA.Pseudouridine at position 55 in tRNA controls the contents of other modified nucleotides for low-temperature adaptation in the extreme-thermophilic eubacterium Thermus thermophilusExamining the Gm18 and m(1)G Modification Positions in tRNA Sequences.Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding.Kinetic characterization of substrate binding sites of thermostable tRNA methyltransferase (TrmB).A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism.
P2860
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P2860
Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes.
description
2006 nî lūn-bûn
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2006年の論文
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name
Functional categorization of t ...... 8) methyltransferase) enzymes.
@en
Functional categorization of the conserved basic amino acid residues in TrmH
@nl
type
label
Functional categorization of t ...... 8) methyltransferase) enzymes.
@en
Functional categorization of the conserved basic amino acid residues in TrmH
@nl
prefLabel
Functional categorization of t ...... 8) methyltransferase) enzymes.
@en
Functional categorization of the conserved basic amino acid residues in TrmH
@nl
P2093
P2860
P356
P1476
Functional categorization of t ...... 8) methyltransferase) enzymes.
@en
P2093
Hiroyuki Hori
Kazunori Watanabe
Osamu Nureki
Shuya Fukai
Yaeta Endo
P2860
P304
34630-34639
P356
10.1074/JBC.M606141200
P407
P577
2006-09-07T00:00:00Z